Please use this identifier to cite or link to this item: http://dspace.aiub.edu:8080/jspui/handle/123456789/602
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dc.contributor.authorOmer, Muhammad-
dc.contributor.authorTariqul Islam, Mohammad-
dc.contributor.authorKhan, Mashooq-
dc.contributor.authorKyoo Kim, Young-
dc.contributor.authorLee, Joon Hyung-
dc.contributor.authorKang, Inn-Kyu-
dc.contributor.authorPark, Soo-Young-
dc.date.accessioned2022-06-14T10:19:21Z-
dc.date.available2022-06-14T10:19:21Z-
dc.date.issued2014-04-23-
dc.identifier.citation14en_US
dc.identifier.issn1598-5032 (Print); 2092-7673 (Online)-
dc.identifier.urihttp://dspace.aiub.edu:8080/jspui/handle/123456789/602-
dc.description.abstractThe interface between a nematic liquid crystal phase, 4-cyano-4-pentylbiphenyl (5CB) and water was examined for protein detection by monitoring the formation of a complex between sodium polystyrene sulfonate (PSSNa) and a positively charged biological species on the 5CB in a transmission electron microscopy (TEM) grid cell coated with a strong anionic polyelectrolyte-containing block copolymer, LCP-b-PSSNa (LCP:poly(4-cyanobi phenyl-4-oxyundecylacrylate)). This block copolymer was successfully synthesized by reversible addition-frag mentation chain transfer polymerization. A monolayer of LCP-b-PSSNa in a Langmuir Blodgett trough (in which PSSNa and LCP were located in and above water, respectively, in the TEM grid cell) was transferred to the 5CB/water interface in the 5CB-filled TEM grid that was already placed on octadecyltrichlorosilane-coated glass. Model proteins such as bovine serum albumin (BSA), hemoglobin (Hb),  chymotrypsinogen-A (ChTg), and lysozyme (LYZ) having different isoelectric points (pIs) were tested for non-specific protein detection. When the protein solu tions were injected into the TEM grid cell, the initial homeotropic orientation of 5CB in the TEM grid cell changed to a planar one below the pIs of the proteins due to electrostatic interactions between PSSNa (- charge) and the pro teins (+ charge); this did not occur above the pIs of the tested proteins. The minimum concentrations at which the homeotropic to planar configurational changes (H-P changes) occurred were 0.02, 0.04, 0.04, and 0.08 wt% for BSA, Hb, ChTg, and LYZ, respectively. Therefore, the positively charged biomaterials were visually detected at the PSSNa-coated LC/water interface during an H-P change by using polarized optical microscopy under crossed polar izers. This simple set-up for non-specific biomaterial detection paves a way for the development of efficient and excellent quality biosensorsen_US
dc.description.sponsorshipThis work was supported by the National Research Foundation of Korea (NRF-2011-0020264)en_US
dc.language.isoenen_US
dc.publisherMacromolecular Research (Elsevier)en_US
dc.relation.ispartofseriesArticle-7;-
dc.subjectstrong anionic polyelectrolyte, poly(4-cyanobiphenyl-4-oxyundecylacrylate)-b-poly(sodium styrene sulfon ate), monolayer, protein, reversible addition-fragmentation polymerization, biosensor.en_US
dc.titleLiquid Crystal-Based Biosensors Using a Strong Polyelectrolyte-Containing Block Copolymer, Poly(4-cyanobiphenyl-4'-oxyundecylacrylate)-b-poly(sodium styrene sulfonate)en_US
dc.typeArticleen_US
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